Figure 2.

L29 is a maize homologue of B. stearothermophilus ribosomal protein L29. (A) The nucleotide sequence and the deduced amino acid sequences are numbered at the left. The two primers used in the DDA are labeled with arrows. Four bases in the AP12 primer did not match the cDNA sequence. The gene-specific primer used in a 5′-RACE reaction is underlined. Three N-myristylation sites are boxed, and four potential protein kinase C phosphorylation sites are marked with asterisks. The boldfaced letters (amino acids 133–136) designate the potential cAMP/cGMP-dependent protein kinase phosphorylation site (accession no. AF 147725). (B) The amino acid alignment of the homologous regions of maize L29, B. stearothermophilus (BACST) and Bacillus subtilis (BACSLI) is shown. Double and single dots indicate amino acid identity and similarity, respectively. Gaps represented by dashes were inserted to maximize the sequence identity. Consensus amino acids are residues that are identical in the three proteins. Numbers in parentheses indicate the position of the start of an amino acid sequence with respect to the initiator methionine of the corresponding protein. B. stearothermophilus L29 exhibited the highest identity with maize L29 of all sequences in the NCBI protein databases at the time of submission. The region of L29 that can be crosslinked to 23S rRNA in ribosomes of B. stearothermophilus (16) are underlined, and the crosslinked lysyl residues are in boldface type (K). Accession numbers for the bacterial L29 proteins shown: B. stearothermophilus (SPIP04457) and B. subtilis (SPIP12873).